在进入和离开大肠杆菌细胞的过程中，OmpT蛋白酶对大肠杆菌素的切割。
Colicin cleavage by OmpT protease during both entry into and release from Escherichia coli cells.
作者信息
Cavard D, Lazdunski C
机构信息
Centre de Biochimie et de Biologie Moléculaire, Centre National de la Recherche Scientifique, Marseille, France.
出版信息
J Bacteriol. 1990 Feb;172(2):648-52. doi: 10.1128/jb.172.2.648-652.1990.
Abstract
Proteolysis of colicins A, E1, E2, and E3 was observed after they were added to whole cells carrying a functional ompT gene. Recombinant plasmid pML19 containing the ompT gene enabled two mutant strains to cleave the added colicins. On the other hand, two colicin A recombinants were split after release from the wild-type bacteria that produced them but not from ompT mutant cells.
摘要
将大肠杆菌素A、E1、E2和E3添加到携带功能性ompT基因的全细胞后，观察到了它们的蛋白水解作用。含有ompT基因的重组质粒pML19使两种突变菌株能够切割添加的大肠杆菌素。另一方面，两种大肠杆菌素A重组体在从产生它们的野生型细菌中释放后会被裂解，但从ompT突变细胞中释放后则不会。
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